| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GDA |
| Uniprot No | Q9Y2T3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-454aa |
| 氨基酸序列 | MCAAQMPPLAHIFRGTFVHSTWTCPMEVLRDHLLGVSDSGKIVFLEEASQ QEKLAKEWCFKPCEIRELSHHEFFMPGLVDTHIHASQYSFAGSSIDLPLL EWLTKYTFPAEHRFQNIDFAEEVYTRVVRRTLKNGTTTACYFATIHTDSS LLLADITDKFGQRAFVGKVCMDLNDTFPEYKETTEESIKETERFVSEMLQ KNYSRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEA VKNLYPSYKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAH CPNSNLSLSSGFLNVLEVLKHEVKIGLGTDVAGGYSYSMLDAIRRAVMVS NILLINKVNEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILI NPKASDSPIDLFYGDFFGDISEAVIQKFLYLGDDRNIEEVYVGGKQVVPF SSSV |
| 预测分子量 | 51 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于GDA重组蛋白的3篇示例参考文献(注：内容为模拟示例，非真实文献)：
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1. **《High-level expression and characterization of recombinant GDA in E. coli》**
*作者：Zhang L., Wang Y., et al.*
**摘要**：研究报道了在大肠杆菌系统中高效表达GDA重组蛋白的优化策略，通过密码子优化和诱导条件调控，获得可溶性蛋白产量提升3倍，并验证其酶活性适用于生物传感器开发。
2. **《Thermostability engineering of GDA recombinant protein for industrial applications》**
*作者：Kumar S., Patel R.K.*
**摘要**：通过定点突变改造GDA重组蛋白的热稳定性，使其在60℃下酶活性保留率从40%提高至85%，为高温工业催化过程提供了更稳定的酶制剂。
3. **《Functional analysis of GDA recombinant antigen in serodiagnosis》**
*作者：Chen X., Li M., et al.*
**摘要**：利用杆状病毒-昆虫细胞系统表达GDA重组抗原，证实其在ELISA检测中特异性识别患者血清抗体，为相关疾病的快速诊断提供了高灵敏度工具。
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如需真实文献，建议通过PubMed或Web of Science以“GDA recombinant protein”或“recombinant GDA expression”为关键词检索，并筛选近五年内发表的论文。
**Background of GDA Recombinant Protein**
Recombinant proteins, engineered through genetic modification, have revolutionized biotechnology and therapeutic development. GDA (Glucose Dehydrogenase from *Alicyclobacillus acidocaldarius*) recombinant protein is a thermally stable enzyme widely studied for its industrial and diagnostic applications. Originally isolated from thermophilic bacteria, native GDA catalyzes the oxidation of glucose to gluconic acid, utilizing NAD(P)+ as a cofactor. However, natural extraction limits scalability and purity, prompting the adoption of recombinant DNA technology for efficient production.
The gene encoding GDA is cloned into expression vectors (e.g., *E. coli* or yeast systems), enabling large-scale synthesis under controlled conditions. Recombinant GDA retains the thermostability (activity up to 70°C) and acid tolerance (pH 4–7) of the wild-type enzyme, making it ideal for harsh industrial processes, such as biosensors, biofuel production, and food processing. Its ability to function without oxygen also supports applications in anaerobic environments.
In diagnostics, GDA is utilized in glucose monitoring systems due to its specificity and stability, offering advantages over glucose oxidase in oxygen-independent reactions. Recent advances focus on protein engineering to enhance catalytic efficiency or modify substrate specificity, broadening its utility. Additionally, structural studies of recombinant GDA provide insights into enzyme mechanics, aiding rational design for tailored applications.
Despite progress, challenges remain in optimizing expression yields and minimizing post-translational modifications in prokaryotic systems. Alternative platforms, like eukaryotic or cell-free systems, are being explored. Overall, GDA recombinant protein exemplifies the synergy between enzymology and genetic engineering, addressing demands for robust biocatalysts in sustainable industries and precision medicine.
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